Evidence map›Paper›PMID 22093547›Full record

ArticleBreast cancer research : BCR2011

Inhibition of cathepsin B activity attenuates extracellular matrix degradation and inflammatory breast cancer invasion.

Bernadette C Victor, Arulselvi Anbalagan, Mona M Mohamed, Bonnie F Sloane, Dora Cavallo-Medved

Open access · goldAbstract read
In one paragraph

Article in Breast cancer research : BCR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.9field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

64 citing papers in PubMed, 114 citations in OpenAlex.

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  14. Cathepsins in neuronal plasticity.Neural regeneration research · 2021
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4 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 3 countries.

Bernadette C VictorDepartment of Pharmacology, Wayne State University, Detroit, Michigan 48201, USA.
Arulselvi Anbalagan
Mona M Mohamed
Bonnie F Sloane
Dora Cavallo-Medved
Wayne State University · USCairo University · EGThe Barbara Ann Karmanos Cancer Institute · USUniversity of Windsor · CA

Funding

Tumor Biology and Microenvironment (Program 1)P30CA022453 · NCI · WAYNE STATE UNIVERSITY · PI PAUL M STEMMER · 1985 to 2026
$68.4M
Proteolytic Pathways in Progression of Pre-Malignant Breast DiseaseR01CA131990 · NCI · WAYNE STATE UNIVERSITY · PI MATTINGLY, RAYMOND R, SLOANE, BONNIE F · 2008 to 2013
$1.9M
Inflammatory Breast Cancer: Factors Contributing to DisseminationR03TW008624 · FIC · WAYNE STATE UNIVERSITY · PI SLOANE, BONNIE F · 2010 to 2012
$179k
FIC NIH HHS R03 TW008624NCI NIH HHS P30CA22453NCI NIH HHS R01 CA131990
6 · The paper itself

Abstract

introductionInflammatory breast cancer (IBC) is an aggressive, metastatic and highly angiogenic form of locally advanced breast cancer with a relatively poor three-year survival rate. Breast cancer invasion has been linked to proteolytic activity at the tumor cell surface. Here we explored a role for active cathepsin B on the cell surface in the invasiveness of IBC.

methodsWe examined expression of the cysteine protease cathepsin B and the serine protease urokinase plasminogen activator (uPA), its receptor uPAR and caveolin-1 in two IBC cell lines: SUM149 and SUM190. We utilized a live cell proteolysis assay to localize in real time the degradation of type IV collagen by IBC cells. IBC patient biopsies were examined for expression of cathepsin B and caveolin-1.

resultsBoth cell lines expressed comparable levels of cathepsin B and uPA. In contrast, levels of caveolin-1 and uPAR were greater in SUM149 cells. We observed that uPA, uPAR and enzymatically active cathepsin B were colocalized in caveolae fractions isolated from SUM149 cells. Using a live-cell proteolysis assay, we demonstrated that both IBC cell lines degrade type IV collagen. The SUM149 cells exhibit predominantly pericellular proteolysis, consistent with localization of proteolytic pathway constitutents to caveolar membrane microdomains. A functional role for cathepsin B was confirmed by the ability of CA074, a cell impermeable and highly selective cathepsin B inhibitor, to significantly reduce pericellular proteolysis and invasion by SUM149 cells. A statistically significant co-expression of cathepsin B and caveolin-1 was found in IBC patient biopsies, thus validating our in vitro data.

conclusionOur study is the first to show that the proteolytic activity of cathepsin B and its co-expression with caveolin-1 contributes to the aggressiveness of IBC.

Indexed as

Cathepsin BCaveolaeCaveolin 1Cell Line, TumorCollagen Type IVDipeptidesExtracellular MatrixFemaleGene Expression Regulation, NeoplasticHumansInflammatory Breast NeoplasmsIntegrin beta ChainsNeoplasm InvasivenessProtein BindingProtein TransportProteolysisCA 074 methyl esterCathepsin BCaveolin 1Collagen Type IVDipeptidesIntegrin beta ChainsReceptors, Urokinase Plasminogen ActivatorUrokinase-Type Plasminogen Activator

Identifiers

PMID22093547
PMCPMC3326557
OpenAlexW2111419151

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.